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O14055 (SYYC_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tyrosine--tRNA ligase, cytoplasmic
EC=6.1.1.1
Alternative name(s):
Tyrosyl-tRNA synthetase
Short name=TyrRS
Gene names
Name:tys1
ORF Names:SPCC1672.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length401 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr) By similarity.

Catalytic activity

ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr).

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtyrosyl-tRNA aminoacylation

Inferred by curator. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tyrosine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401Tyrosine--tRNA ligase, cytoplasmic
PRO_0000055675

Regions

Motif42 – 509"HIGH" region
Motif220 – 2245"KMSKS" region

Sites

Binding site371Tyrosine By similarity
Binding site1641Tyrosine By similarity
Binding site1681Tyrosine By similarity
Binding site1711Tyrosine By similarity
Binding site1861Tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
O14055 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 2BD9E0FA6C2172DE

FASTA40144,576
        10         20         30         40         50         60 
MSLTPDEKYE LITRNLQEVL GAKMIREILN ERDISLYWGS APTGRPHCGY FVPMMKLADF 

        70         80         90        100        110        120 
LKAGVHVTVL LADVHAFLDN MKAPMELVQH RVRYYEIIVK SILKSLNIPI EKLRFVIGSS 

       130        140        150        160        170        180 
YQLKEDYTLD NFRLAASTTE HTARRAGAEV VKQVASPLLS SLIYPGMQAL DEQYLGVDVQ 

       190        200        210        220        230        240 
FGGVDQRKIF VMAEEVLPVL GYKKRGHLMN PMVPSLAGGK MSSSAAANAK IDILDDPKTV 

       250        260        270        280        290        300 
NKKIRSAFCE PGVVEENGCL AFLKYVSFPA MELRGETEFV IDRPEQFGGR MVFKTYEEVE 

       310        320        330        340        350        360 
KAYKDLTLSP QDLKLGLESS VNTLLAGVQE QLKQYPDLDS ILKAAYPDPK DLKKAMKQKK 

       370        380        390        400 
QDKKNAKKAG TTNASIAAES GAAPATESQT AESFKKLNLD D

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329672 Genomic DNA. Translation: CAA20443.1.
PIRT41049.
RefSeqNP_587876.1. NM_001022868.1.

3D structure databases

ProteinModelPortalO14055.
SMRO14055. Positions 4-347.
ModBaseSearch...

Protein-protein interaction databases

STRINGO14055.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1672.05c.1; SPCC1672.05c.1:pep; SPCC1672.05c.
GeneID2539269.
GenomeReviewsGene locus tys1 in contig CU329672_GR.
KEGGspo:SPCC1672.05c.
NMPDRfig|4896.1.peg.214.

Organism-specific databases

GeneDB_SpombeSPCC1672.05c.

Phylogenomic databases

eggNOGfuNOG04409.
GeneTreeEFGT00050000004557.
HOGENOMHBG330667.
OMAYIGFEIS.
OrthoDBEOG43R6W6.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-002221-MONOMER.

Gene expression databases

ArrayExpressO14055.

Family and domain databases

InterProIPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002307. Tyr-tRNA-synth.
IPR023617. Tyr-tRNA-synth_arc-type.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01866.
PANTHERPTHR11946:SF8. Tyr-tRNA_synth. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PIRSFPIRSF006588. TyrRS_arch_euk. 1 hit.
PRINTSPR01040. TRNASYNTHTYR.
TIGRFAMsTIGR00234. TyrS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYYC_SCHPO
AccessionPrimary (citable) accession number: O14055
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: January 25, 2012
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

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